ID K9LV95_9EUPU Unreviewed; 170 AA. AC K9LV95; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 18-SEP-2013, entry version 5. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COI; OS Oxyloma sp. HWH-2012. OG Mitochondrion. OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda; OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; OC Stylommatophora; Sigmurethra; Succineoidea; Succineidae; Oxyloma. OX NCBI_TaxID=1216502; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=12-2; RA Culver M., Miller M., Roth B., Sorensen J., Herrmann H.-W.; RT "Investigation of anatomical and genetic variation within western RT Oxyloma (Pulmonata: Succineidae) with respect to the federally RT endangered Kanab ambersnail (Oxyloma haydeni kanabense)."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B (By similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JN716965; AFP27945.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; Cyt_c_Oxase_su1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; COX1; 1. DR PROSITE; PS50855; COX1; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Respiratory chain; Transmembrane; Transport. FT NON_TER 1 1 FT NON_TER 170 170 SQ SEQUENCE 170 AA; 18416 MW; C80988165FDCB9CB CRC64; ELGTSAVLLD DHLYNVIVTA HAFVMIFFMV MPIMIGGFGN WMVPLMIGAP DMSFPRMNNM SFWLLPPSFV LLLCSSMVEG GAGTGWTVYP PLSSLTGHSG ASVDLAIFSL HLAGISSILG AINFITTIFN MRQLGMTMER LSLFVWSILV TVFLLLLSLP VLAGAITMLL //